2zwt

Publication Abstract from PubMed

The binding of (+)-camphor to cytochrome P450cam (P450cam) expels a cluster of waters at the active site, raising the redox potential of the haem to an extent that allows reduction by the electron-transfer system. This binding was reported to involve no significant structural changes in the protein. Here, two ferric P450cam structures partially complexed with (+)-camphor were determined by X-ray crystallography at 1.30-1.35 A resolution, revealing the structures of the substrate-free and substrate-bound forms. (+)-Camphor binding induces rotation of Thr101 to form a hydrogen bond that acts as a hydrogen donor to a peripheral haem propionate. This bonding contributes to the redox-potential change.

Substrate binding induces structural changes in cytochrome P450cam.,Sakurai K, Shimada H, Hayashi T, Tsukihara T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt, 2):80-3. Epub 2009 Jan 31. PMID:19193991^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.